A typical protein crystal at room temperature only survives a fraction of the X-ray dose required for a complete high-resolution data set before it becomes irrevocably radiation-damaged. To inhibit the occurrence of radiation damage, protein crystals containing water surrounding and inside the crystals are typically flash cooled at atmospheric pressure. The goal is to obtain amorphous ice rather than crystalline ice and to reduce the damage on the crystal by the cryofreezing process. Cryoprotectants are typically added to promote the result. In practice, cryoprotectants that work with one protein do not work with another, requiring a trial-and-error search. This process is time consuming and in some cases unsuccessful.